SitesBLAST
Comparing WP_015739819.1 NCBI__GCF_000024605.1:WP_015739819.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
F9VMT6 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; Fructose-1,6-bisphosphatase; FBPase; EC 3.1.3.11; EC 4.1.2.13 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see 2 papers)
61% identity, 95% coverage: 3:359/376 of query aligns to 2:361/384 of F9VMT6
- D11 (= D12) binding ; mutation to A: 930-fold decrease in FBPase catalytic efficiency.
- H18 (= H19) binding in other chain; binding ; binding ; mutation to A: 1.7-fold increase in FBPase catalytic activity and 5-fold decrease in FBP affinity, leading to a 2.7-fold decrease in FBPase catalytic efficiency.
- D52 (= D50) binding ; binding ; mutation to A: 175-fold decrease in FBPase catalytic efficiency.
- D53 (= D51) binding ; mutation to A: 1000-fold decrease in FBPase catalytic activity.
- Y90 (= Y88) binding in other chain
- Q94 (= Q92) binding ; mutation to A: 1.3-fold increase in FBPase catalytic efficiency.
- GN 103:104 (= GN 101:102) binding in other chain
- D131 (= D129) binding ; mutation to A: 2-fold increase in FBP affinity and 10-fold decrease in FBPase catalytic activity, leading to a 5.5-fold decrease in FBPase catalytic efficiency.
- K132 (= K130) binding in other chain; binding
- Y228 (= Y226) mutation to F: Retains the FBPase activity, but loses the FBP aldolase activity.
- K231 (= K229) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity; binding
- D232 (= D230) binding ; binding ; mutation to A: 275-fold decrease in FBPase catalytic activity.
- D233 (= D231) binding ; binding ; mutation to A: 2000-fold decrease in FBPase catalytic activity.
- QH 241:242 (≠ QN 239:240) binding
- R265 (= R263) binding in other chain; binding
- D286 (= D284) binding in other chain; binding
- Y347 (= Y345) binding in other chain
1umgA Crystal structure of fructose-1,6-bisphosphatase (see paper)
61% identity, 95% coverage: 3:359/376 of query aligns to 1:357/359 of 1umgA
- binding 1,6-fructose diphosphate (linear form): H17 (= H19), D51 (= D50), Y89 (= Y88), Q93 (= Q92), S101 (= S100), G102 (= G101), N103 (= N102), K131 (= K130), D228 (= D230), D229 (= D231), M260 (= M262), R261 (= R263), D282 (= D284), Y343 (= Y345)
- binding magnesium ion: D10 (= D12), H17 (= H19), D51 (= D50), D51 (= D50), D52 (= D51), Q93 (= Q92), D130 (= D129), D228 (= D230), D229 (= D231), D229 (= D231)
B1YAL1 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; EC 3.1.3.11; EC 4.1.2.13 from Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta) (Thermoproteus neutrophilus) (see paper)
59% identity, 94% coverage: 3:356/376 of query aligns to 2:369/399 of B1YAL1
- D11 (= D12) binding
- H18 (= H19) binding in other chain; binding ; binding
- D52 (= D50) binding ; binding
- D53 (= D51) binding
- Y91 (= Y88) binding in other chain
- Q95 (= Q92) binding
- GN 104:105 (= GN 101:102) binding in other chain
- D132 (= D129) binding
- K133 (= K130) binding in other chain; binding
- Y229 (= Y226) mutation to F: Shows unaltered FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
- K232 (= K229) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity
- D233 (= D230) binding ; binding
- D234 (= D231) binding ; binding
- QS 242:243 (≠ QN 239:240) binding
- R266 (= R263) binding in other chain; binding
- D297 (= D284) binding in other chain; binding ; mutation to N: 18-fold decrease in FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
- Y358 (= Y345) binding in other chain
3t2dA Fructose-1,6-bisphosphate aldolase/phosphatase from thermoproteus neutrophilus, fbp-bound form (see paper)
59% identity, 94% coverage: 3:356/376 of query aligns to 2:369/390 of 3t2dA
- binding magnesium ion: D11 (= D12), H18 (= H19), D52 (= D50), D52 (= D50), D53 (= D51), Q95 (= Q92), D132 (= D129), D233 (= D230), D234 (= D231), D234 (= D231)
- binding 1,6-di-O-phosphono-D-fructose: H18 (= H19), D52 (= D50), Y91 (= Y88), Q95 (= Q92), S103 (= S100), G104 (= G101), N105 (= N102), K133 (= K130), D233 (= D230), D234 (= D231), M265 (= M262), R266 (= R263), D297 (= D284), Y358 (= Y345)
3t2eA Fructose-1,6-bisphosphate aldolase/phosphatase from thermoproteus neutrophilus, f6p-bound form (see paper)
58% identity, 94% coverage: 3:356/376 of query aligns to 2:365/385 of 3t2eA
- binding fructose -6-phosphate: H18 (= H19), Y91 (= Y88), M261 (= M262), R262 (= R263), D293 (= D284), Y354 (= Y345)
- binding magnesium ion: D11 (= D12), H18 (= H19), D52 (= D50), D52 (= D50), D53 (= D51), Q95 (= Q92), D132 (= D129), D230 (= D231)
A0RV30 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; EC 3.1.3.11; EC 4.1.2.13 from Cenarchaeum symbiosum (strain A) (see 2 papers)
45% identity, 91% coverage: 3:345/376 of query aligns to 2:342/376 of A0RV30
- Y224 (= Y226) mutation to F: Shows slightly decreased FBP phosphatase activity, whereas FBP aldolase activity is nearly completely abolished.
- K227 (= K229) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity; mutation to R: Shows enhanced FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
- D228 (= D230) mutation to N: Shows completely abolition of both FBP aldolase and FBP phosphatase activities.
- E341 (= E344) mutation to Q: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished.
- Y342 (= Y345) mutation to F: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished.
Query Sequence
>WP_015739819.1 NCBI__GCF_000024605.1:WP_015739819.1
MAKVTLSVIKADIGGFVGHSAVHPEVKEKARACLEKHPLLIDYYVAHVGDDLVLIMTHEH
GRNKGEIHKLAWDTFVACTEVAKKLKLYGAGQDLLADAFSGNVKGLGPGVAEMEVEERES
EPVVVLMADKTEPGAWNLPLYKIFADPFNTIGLIIDPKMHCGFAFEVRDLIEDKKIIFNA
PEDLYDMLVFIGAPGRYAIKRVFHRGTGEIAAVSSTQRLNLMAGRYVGKDDPVCIVRCQN
GYPSVGEVLEPFAFPHLVSGWMRGSHSGPLMPVSMDDARPTRFDGPPRVVALGFQLADGK
LIGPNDFFSDPAFDNARRLALEIADYLRRLGPFEPHRLHLDEMEYTTMPQVMEKLRDRFI
DLRLAKKARAAAGGEA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory